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Conserved domains on  [gi|1819699085|ref|WP_165369383|]
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glycosyltransferase family 4 protein [Escherichia coli]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133538)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
7-372 1.60e-120

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


:

Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 353.05  E-value: 1.60e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085   7 KLCYFINSDWYFDLHWTDRAIAARDAGYEIHIISHfVDDKIAEKFRTLGFVCHNIPLVAQSFNVLIFFRAFSKARKIIQN 86
Cdd:cd03808     1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAP-DGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  87 INPDLLHCITIKPCLIGGFLAKSTHRP-VILSFVGLGRVFSAEsaclKLLRSFTVMAYKyIASNKCSLFMFEHDKDRAKL 165
Cdd:cd03808    80 EKPDIVHCHTPKPGILGRLAARLAGVPkVIYTVHGLGFVFTEG----KLLRLLYLLLEK-LALLFTDKVIFVNEDDRDLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 166 ADLVGIDYKQTIVIDGAGINPEIYKYSLEQQR-DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDK 244
Cdd:cd03808   155 IKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPsEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 245 DAIplaTIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLI 324
Cdd:cd03808   235 SEI---LIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFL 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1819699085 325 VKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTL 372
Cdd:cd03808   311 VPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
7-372 1.60e-120

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 353.05  E-value: 1.60e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085   7 KLCYFINSDWYFDLHWTDRAIAARDAGYEIHIISHfVDDKIAEKFRTLGFVCHNIPLVAQSFNVLIFFRAFSKARKIIQN 86
Cdd:cd03808     1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAP-DGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  87 INPDLLHCITIKPCLIGGFLAKSTHRP-VILSFVGLGRVFSAEsaclKLLRSFTVMAYKyIASNKCSLFMFEHDKDRAKL 165
Cdd:cd03808    80 EKPDIVHCHTPKPGILGRLAARLAGVPkVIYTVHGLGFVFTEG----KLLRLLYLLLEK-LALLFTDKVIFVNEDDRDLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 166 ADLVGIDYKQTIVIDGAGINPEIYKYSLEQQR-DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDK 244
Cdd:cd03808   155 IKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPsEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 245 DAIplaTIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLI 324
Cdd:cd03808   235 SEI---LIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFL 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1819699085 325 VKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTL 372
Cdd:cd03808   311 VPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
198-357 2.40e-24

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 97.73  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 198 DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDKdaiPLATIQKWQSEGVINWLGHCSN--VFDLIE 275
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR---LKKLAEKLGLGDNVIFLGFVSDedLPELLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 276 ESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGR 355
Cdd:pfam00534  78 IADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156

                  ..
gi 1819699085 356 KR 357
Cdd:pfam00534 157 KR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
269-380 7.92e-22

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 89.66  E-value: 7.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 269 NVFDLIE----ESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNP 344
Cdd:COG0438     9 GLDLLLEallaAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDP 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819699085 345 ETRVAMGINGRKRIQDKFSSVMIINKTLKTYLDVVE 380
Cdd:COG0438    88 ELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
203-337 8.91e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 43.93  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 203 LFASRMLW--SKGLGDLIEAkkiLSNKNIHFTLNVAGilvENDKDAIPLATIQKWQSEGVINWLGHCSN----VFDLIEE 276
Cdd:PRK09922  184 LYVGRLKFegQKNVKELFDG---LSQTTGEWQLHIIG---DGSDFEKCKAYSRELGIEQRIIWHGWQSQpwevVQQKIKN 257
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819699085 277 SNIVALPSVYaEGVPRILLEASSVGRACIAYD-VGGCDSLIINNYNGLIVKSKSVEELAEKL 337
Cdd:PRK09922  258 VSALLLTSKF-EGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKL 318
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
7-372 1.60e-120

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 353.05  E-value: 1.60e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085   7 KLCYFINSDWYFDLHWTDRAIAARDAGYEIHIISHfVDDKIAEKFRTLGFVCHNIPLVAQSFNVLIFFRAFSKARKIIQN 86
Cdd:cd03808     1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAP-DGDKLSDELKELGVKVIDIPILRRGINPLKDLKALFKLYKLLKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  87 INPDLLHCITIKPCLIGGFLAKSTHRP-VILSFVGLGRVFSAEsaclKLLRSFTVMAYKyIASNKCSLFMFEHDKDRAKL 165
Cdd:cd03808    80 EKPDIVHCHTPKPGILGRLAARLAGVPkVIYTVHGLGFVFTEG----KLLRLLYLLLEK-LALLFTDKVIFVNEDDRDLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 166 ADLVGIDYKQTIVIDGAGINPEIYKYSLEQQR-DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDK 244
Cdd:cd03808   155 IKKGIIKKKKTVLIPGSGVDLDRFQYSPESLPsEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 245 DAIplaTIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLI 324
Cdd:cd03808   235 SEI---LIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFL 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1819699085 325 VKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTL 372
Cdd:cd03808   311 VPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
25-380 1.27e-38

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 141.91  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  25 RAIAARdaGYEIHIISHFVDDKIAEKFRTLGFVchniPLVAQSFNVLIFFRAFSKARKIIQNINPDLLHCITIKPCLIGG 104
Cdd:cd03801    25 RALAAR--GHDVTVLTPADPGEPPEELEDGVIV----PLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 105 FLAKSTHRPVILSFVGL--GRVFSAESACLKLLRSFTVMAYKYIASNKCSLFMfehdkdRAKLADLVGIDYKQTIVIdGA 182
Cdd:cd03801    99 LLALLLGAPLVVTLHGAepGRLLLLLAAERRLLARAEALLRRADAVIAVSEAL------RDELRALGGIPPEKIVVI-PN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 183 GINPEIY----KYSLEQQRDVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGilvenDKDAIP--LATIQKWQ 256
Cdd:cd03801   172 GVDLERFspplRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG-----GDGPLRaeLEELELGL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 257 SEGVInWLGHCSN--VFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELA 334
Cdd:cd03801   247 GDRVR-FLGFVPDeeLPALYAAADVFVLPSRY-EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALA 324
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1819699085 335 EKLGFLLDNPETRVAMGINGRKRIQDKFSsvmiINKTLKTYLDVVE 380
Cdd:cd03801   325 DALLRLLADPELRARLGRAARERVAERFS----WERVAERLLDLYR 366
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
31-370 6.84e-27

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 109.63  E-value: 6.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  31 DAGYEIHIISHF---------VDDKIaeKFRTLGfvchnIPLVAQSFNVLIFFRAFSKARKIIQNINPD----------- 90
Cdd:cd03820    28 KKGYDVTIISLDsaekppfyeLDDNI--KIKNLG-----DRKYSHFKLLLKYFKKVRRLRKYLKNNKPDvvisfrtsllt 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  91 LLHCITIKPCLIGGFLAKSTHRPVILSFVGLGRVfsaesaCLKLLRSFTVMAykyiasnkcslfmfEHDKDRAKladlvG 170
Cdd:cd03820   101 FLALIGLKSKLIVWEHNNYEAYNKGLRRLLLRRL------LYKRADKIVVLT--------------EADKLKKY-----K 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 171 IDYKQTIVIDgagiNP-----EIYKYSLEQQRdvpvVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGilVENDKD 245
Cdd:cd03820   156 QPNSNVVVIP----NPlsfpsEEPSTNLKSKR----ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG--DGPERE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 246 AIpLATIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDvggCDS----LIINNYN 321
Cdd:cd03820   226 EL-EKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFD---CPTgpseIIEDGEN 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1819699085 322 GLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIqDKFSSVMIINK 370
Cdd:cd03820   301 GLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA-ERFSIEKIIKQ 348
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
29-375 8.82e-25

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 103.94  E-value: 8.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  29 ARDAGYEIHIISHFVDDKIAEKFRTLGfvCHNIPLVAQSFNVLiffRAFSKARKIIQNINPDLLHCITIKPCLIGGFLAK 108
Cdd:cd03807    25 MDKSRFEHVVISLTGDGVLGEELLAAG--VPVVCLGLSSGKDP---GVLLRLAKLIRKRNPDVVHTWMYHADLIGGLAAK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 109 STH-RPVILSfvglgRVFSAESAC-------LKLLRSFTVMAYKYIASnkcslfmfehdkDRAKLADLVGIDYKQTIVID 180
Cdd:cd03807   100 LAGgVKVIWS-----VRSSNIPQRltrlvrkLCLLLSKFSPATVANSS------------AVAEFHQEQGYAKNKIVVIY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 181 GaGINPEIYKYSLEQQ----------RDVPVVLFASRMLWSKGLGDLIEAKKIL--SNKNIHFTLNVAGILVENdkdaiP 248
Cdd:cd03807   163 N-GIDLFKLSPDDASRararrrlglaEDRRVIGIVGRLHPVKDHSDLLRAAALLveTHPDLRLLLVGRGPERPN-----L 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 249 LATIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCdSLIINNYNGLIVKSK 328
Cdd:cd03807   237 ERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRT-EGFPNALLEAMACGLPVVATDVGGA-AELVDDGTGFLVPAG 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1819699085 329 SVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTLKTY 375
Cdd:cd03807   315 DPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLY 361
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
198-357 2.40e-24

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 97.73  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 198 DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDKdaiPLATIQKWQSEGVINWLGHCSN--VFDLIE 275
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR---LKKLAEKLGLGDNVIFLGFVSDedLPELLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 276 ESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGR 355
Cdd:pfam00534  78 IADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENAR 156

                  ..
gi 1819699085 356 KR 357
Cdd:pfam00534 157 KR 158
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
60-355 1.51e-22

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 97.04  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  60 NIPLVAQSFNVLIFFRAFSKARKIIQNINPDLLHCITIKPCLIGGFLAKSTHRPVILSFVGLGRVFSAESACLKLLRSFT 139
Cdd:cd03819    48 GIGLPGLKVPLLRALLGNVRLARLIRRERIDLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARG 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 140 vmAYKYIASNKCSLFMFEHDK-DRAKLADLV-GIDYKQTiviDGAGINPEIYKYSLEqqRDVPVVLFASRMLWSKGLGDL 217
Cdd:cd03819   128 --DRVIAVSELVRDHLIEALGvDPERIRVIPnGVDTDRF---PPEAEAEERAQLGLP--EGKPVVGYVGRLSPEKGWLLL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 218 IEAKKILsNKNIHFTLNVAGILVENDKDAiplATIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEA 297
Cdd:cd03819   201 VDAAAEL-KDEPDFRLLVAGDGPERDEIR---RLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLH-EEFGRVALEA 275
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1819699085 298 SSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGR 355
Cdd:cd03819   276 MACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAA 333
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
269-380 7.92e-22

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 89.66  E-value: 7.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 269 NVFDLIE----ESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNP 344
Cdd:COG0438     9 GLDLLLEallaAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDP 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819699085 345 ETRVAMGINGRKRIQDKFSSVMIINKTLKTYLDVVE 380
Cdd:COG0438    88 ELRRRLGEAARERAEERFSWEAIAERLLALYEELLA 123
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
200-343 5.52e-21

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 87.95  E-value: 5.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 200 PVVLFASRML-WSKGLGDLIEAKKILSNKNIHFTLNVAGilvenDKDAIPLATIQKWQSEGVInWLGHCSNVFDLIEESN 278
Cdd:pfam13692   2 PVILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVG-----DGPEEELEELAAGLEDRVI-FTGFVEDLAELLAAAD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819699085 279 IVALPSVYaEGVPRILLEASSVGRACIAYDVGGCdSLIINNYNGLIVKSKSVEELAEKLGFLLDN 343
Cdd:pfam13692  76 VFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGI-PELVDGENGLLVPPGDPEALAEAILRLLED 138
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
26-347 3.44e-20

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 90.50  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  26 AIAARDAGYEIHIIShFVDDKIAEKFRTLGFVCHNIPLVAQSFNVLIFFRAFSKARKIIQNINPDLLHCITIKPCLIGGF 105
Cdd:cd03811    22 ANALDKRGYDVTLVL-LRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVISFLGFATYIVAK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 106 LAKStHRPVI----LSFVGLGRVFSAESACLKLLRSFTvmayKYIAsnkCSLFMfehdkdrAKLADLVGIDYKQTIV--- 178
Cdd:cd03811   101 LAAA-RSKVIawihSSLSKLYYLKKKLLLKLKLYKKAD----KIVC---VSKGI-------KEDLIRLGPSPPEKIEviy 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 179 --IDGAGINPEIYKYSLEQQRDVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGilvENDKDAIPLATIQKWQ 256
Cdd:cd03811   166 npIDIDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG---DGPLREELEKLAKELG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 257 SEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEK 336
Cdd:cd03811   243 LAERVIFLGFQSNPYPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGI 321
                         330
                  ....*....|.
gi 1819699085 337 LGFLLDNPETR 347
Cdd:cd03811   322 LAALLQKKLDA 332
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
173-378 2.17e-17

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 82.81  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 173 YKQTIVIDGAGINPEIYKYSLEQQR---DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGilvendkDAIPL 249
Cdd:cd03798   171 PRDRVDVIPNGVDPARFQPEDRGLGlplDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVG-------DGPLR 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 250 ATIQKWQSEGVinwLGHCSNVFDLI--EE-------SNIVALPSvYAEGVPRILLEASSVGRACIAYDVGGCDSLIINNY 320
Cdd:cd03798   244 EALRALAEDLG---LGDRVTFTGRLphEQvpayyraCDVFVLPS-RHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPE 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1819699085 321 NGLIVKSKSVEELAEKLGFLLDNPETRVaMGINGRKRIQDKFSSVMIINKTLKTYLDV 378
Cdd:cd03798   320 TGLLVPPGDADALAAALRRALAEPYLRE-LGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
177-362 3.54e-17

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 81.73  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 177 IVIDGAGINPEIYKYSLEQ-QRDVPV-VLFASRMLWSKGLGDLIEAKKILSNK--NIHFTLNVAGILVENDKDAIplati 252
Cdd:cd03799   150 IIVHRSGIDCNKFRFKPRYlPLDGKIrILTVGRLTEKKGLEYAIEAVAKLAQKypNIEYQIIGDGDLKEQLQQLI----- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 253 QKWQSEGVINWLG--HCSNVFDLIEESNIVALPSVYA-----EGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIV 325
Cdd:cd03799   225 QELNIGDCVKLLGwkPQEEIIEILDEADIFIAPSVTAadgdqDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLV 304
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1819699085 326 KSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKF 362
Cdd:cd03799   305 PERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
90-376 5.31e-17

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 82.00  E-value: 5.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  90 DLLHCI-TIKPCLIGGFLAKSTHRPVILSFVGlgrVFSAESAcLKLLRSFTVMAY---------------KYIASNKC-S 152
Cdd:cd03813   175 DLYHSVsTGYAGLLGALARHRRGIPFLLTEHG---IYTRERK-IEILQSTWIMGYikklwirfferlgklAYQQADKIiS 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 153 LFmfEHDKDRAKLadlVGIDYKQTIVIDGaGINPEIYKYSLEQQ--RDVPVVLFASRMLWSKGLGDLIEAKKILSNKNIH 230
Cdd:cd03813   251 LY--EGNRRRQIR---LGADPDKTRVIPN-GIDIQRFAPAREERpeKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPD 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 231 FTLNVAGILVEND------KDAIPLATIQkwqsEGVInWLGHcSNVFDLIEESNIVALPSVyAEGVPRILLEASSVGRAC 304
Cdd:cd03813   325 AEGWLIGPEDEDPeyaqecKRLVASLGLE----NKVK-FLGF-QNIKEYYPKLGLLVLTSI-SEGQPLVILEAMASGVPV 397
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819699085 305 IAYDVGGCDSLIINNYN-----GLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTLKTYL 376
Cdd:cd03813   398 VATDVGSCRELIYGADDalgqaGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
165-378 4.04e-14

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 72.75  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 165 LADLV---GIDYKQTIVIDGAGINPEI--------YKYSLEQQRDVPVVLFASRML--WSKGLGDLIEAKKILSNKNIhF 231
Cdd:cd03825   148 LADMVrrsPLLKGLPVVVIPNGIDTEIfapvdkakARKRLGIPQDKKVILFGAESVtkPRKGFDELIEALKLLATKDD-L 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 232 TLNVAGILVENDKDAiplatiqkwqsEGVINWLGHCSNVFDLIEESN---IVALPSvYAEGVPRILLEASSVGRACIAYD 308
Cdd:cd03825   227 LLVVFGKNDPQIVIL-----------PFDIISLGYIDDDEQLVDIYSaadLFVHPS-LADNLPNTLLEAMACGTPVVAFD 294
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 309 VGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTLKTYLDV 378
Cdd:cd03825   295 TGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
200-364 5.97e-14

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 72.31  E-value: 5.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 200 PVVLFASRMLWSKGLGDLIEAKKILsnkNIHFTLNVAGILVENDKDAIPLATIQKwqsegvINWLGHCSNV--FDLIEES 277
Cdd:cd03795   192 KIFLFIGRLVYYKGLDYLIEAAQYL---NYPIVIGGEGPLKPDLEAQIELNLLDN------VKFLGRVDDEekVIYLHLC 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 278 NIVALPSVY-AEGVPRILLEASSVGRACIAYDVGGCDSLIINN-YNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGR 355
Cdd:cd03795   263 DVFVFPSVLrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNgETGLVVPPKDPDALAEAIDKLLSDEELRESYGENAK 342

                  ....*....
gi 1819699085 356 KRIQDKFSS 364
Cdd:cd03795   343 KRFEELFTA 351
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
9-363 6.61e-13

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 69.29  E-value: 6.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085   9 CYFINSDWYFDLHWTDRAIAARDAGYEIHIISHFVDDKIAEKFRTLGFVCHNIPLV------------------AQSFNV 70
Cdd:cd03794     7 QYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATETKDGIRVIrvklgpikknglirrllnYLSFAL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  71 LIFFRAFSKARKiiqninPDLLHCITIKP--CLIGGFLAKSTHRPVIL--------SFVGLGrvFSAESACLKLLRSFTV 140
Cdd:cd03794    87 AALLKLLVREER------PDVIIAYSPPItlGLAALLLKKLRGAPFILdvrdlwpeSLIALG--VLKKGSLLKLLKKLER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 141 MAYKyiASNKCSLfmfeHDKDRAKLADLVGIDYKQTIVIDgAGINPEIYKYSLEQQ-------RDVPVVLFASRMLWSKG 213
Cdd:cd03794   159 KLYR--LADAIIV----LSPGLKEYLLRKGVPKEKIIVIP-NWADLEEFKPPPKDElrkklglDDKFVVVYAGNIGKAQG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 214 LGDLIEA-KKILSNKNIHFTLNVAGILVENDKDAIPLATIQKWQSEGVINWlghcSNVFDLIEESNIVALP----SVYAE 288
Cdd:cd03794   232 LETLLEAaERLKRRPDIRFLFVGDGDEKERLKELAKARGLDNVTFLGRVPK----EEVPELLSAADVGLVPlkdnPANRG 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819699085 289 GVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFS 363
Cdd:cd03794   308 SSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEKFS 382
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
197-363 9.75e-12

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 65.72  E-value: 9.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 197 RDVPVVLFASRMLWSKGLGDLIEA----KKILSNKNIHFtlnVAGILVEN-DKDAIPLATIQKwqSEGVI---NWLGHCS 268
Cdd:cd03800   218 PDKPVVLALGRLDPRKGIDTLVRAfaqlPELRELANLVL---VGGPSDDPlSMDREELAELAE--ELGLIdrvRFPGRVS 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 269 --NVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPET 346
Cdd:cd03800   293 rdDLPELYRAADVFVVPSLY-EPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPAL 371
                         170
                  ....*....|....*..
gi 1819699085 347 RVAMGINGRKRIQDKFS 363
Cdd:cd03800   372 WQRLSRAGLERARAHYT 388
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
198-362 1.11e-11

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 65.55  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 198 DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAG---ILVENDKDAIPLATIQkwqsegVINWLGHcSNVFDLI 274
Cdd:cd05844   188 RAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGdgpLRPALQALAAALGRVR------FLGALPH-AEVQDWM 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 275 EESNIVALPSVYA-----EGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVA 349
Cdd:cd05844   261 RRAEIFCLPSVTAasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADR 340
                         170
                  ....*....|...
gi 1819699085 350 MGINGRKRIQDKF 362
Cdd:cd05844   341 MGGAARAFVCEQF 353
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
203-325 3.30e-11

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.81  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 203 LFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDKDAIPLATIQKWQSEGVINWLGHCSNVFDLIEESNIVAL 282
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1819699085 283 PSvYAEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIV 325
Cdd:cd01635   194 PS-RSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
145-363 6.56e-11

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 62.70  E-value: 6.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 145 YIASNKCSLFMFEH-DKDRA--------KLADLVGIDYKQTIVIDGAGINPEIYKYSLEQQRDVPVVLFASRMLWSKGLG 215
Cdd:cd04949    97 HSLIKNFYKYVFENlNKYDAiivsteqqKQDLSERFNKYPPIFTIPVGYVDQLDTAESNHERKSNKIITISRLAPEKQLD 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 216 DLIEAKKILSNKNIHFTLNVAGilvENDKDAIPLATIQKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILL 295
Cdd:cd04949   177 HLIEAVAKAVKKVPEITLDIYG---YGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQM-EGFGLTLM 252
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819699085 296 EASSVGRACIAYDVG-GCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKrIQDKFS 363
Cdd:cd04949   253 EAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYK-IAEKYS 320
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
7-122 8.57e-11

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 59.26  E-value: 8.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085   7 KLCYFINSDWYFDLHWTDraiAARDAGYEIHIIS---HFVDDKIAEKFRtlgFVCHNIPlvaqSFNVLIFFRAFsKARKI 83
Cdd:pfam13477   1 KILLLANADSIHTLRWAD---ALADRGYDVHVISskgPAKDELIAEGIH---VHRLKVP----RKGPLGYLKAF-RLKKL 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1819699085  84 IQNINPDLLHCITIKPC-LIGGFLAK-STHRPVILSFVGLG 122
Cdd:pfam13477  70 IKKIKPDVVHVHYAKPYgLLAGLAARlSGFPPVVLSAWGLD 110
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
183-356 2.40e-10

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 61.62  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 183 GINPEIYKYSLEQQR------DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGilvENDKDaiPLATIQKWQ 256
Cdd:cd03821   182 GVDIPEFDPGLRDRRkhngleDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG---PDDGA--YPAFLQLQS 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 257 SEGV---INWLGHCSNVfDLIE---ESNIVALPSvYAEGVPRILLEASSVGR-ACIAYDVGGCDslIINNYNGLIVKSkS 329
Cdd:cd03821   257 SLGLgdrVTFTGPLYGE-AKWAlyaSADLFVLPS-YSENFGNVVAEALACGLpVVITDKCGLSE--LVEAGCGVVVDP-N 331
                         170       180
                  ....*....|....*....|....*..
gi 1819699085 330 VEELAEKLGFLLDNPETRVAMGINGRK 356
Cdd:cd03821   332 VSSLAEALAEALRDPADRKRLGEMARR 358
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
25-363 1.03e-09

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 59.30  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  25 RAIAARDAGYEIHIISHFVDDKIAEKFRTLGFVCHNIPLVAQSFNVLIFFRAfskaRKIIQNINPDLLHCitikPCLIGG 104
Cdd:cd03809    25 KALAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQ----ILLPKKDKPDLLHS----PHNTAP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 105 FLAKSthRPVIL-----------SFVGLGRVFSAESACLKLLRSftvmAYKYIASNKCSlfmfehdkdRAKLADLVGIDY 173
Cdd:cd03809    97 LLLKG--CPQVVtihdliplrypEFFPKRFRLYYRLLLPISLRR----ADAIITVSEAT---------RDDIIKFYGVPP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 174 KQTIVIdGAGINPEIYKY------SLEQQRDVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILveNDKDAI 247
Cdd:cd03809   162 EKIVVI-PLGVDPSFFPPesaavlIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGK--GWEDEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 248 PLATIQKWQSEGVINWLGHCSN--VFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGgcdSL-IINNYNGLI 324
Cdd:cd03809   239 LLDLVKKLGLGGRVRFLGYVSDedLPALYRGARAFVFPSLY-EGFGLPVLEAMACGTPVIASNIS---VLpEVAGDAALY 314
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1819699085 325 VKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQdKFS 363
Cdd:cd03809   315 FDPLDPESIADAILRLLEDPSLREELIRKGLERAK-KFS 352
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
81-358 2.56e-09

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 58.11  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  81 RKIIQNINPDLLHCitikPCLIGgflaksthrpvilsfVGLGRVFSAESACLKLLrsFTVMAYKYIASNKcslFMFEHDK 160
Cdd:cd03823    89 ARLLEDFRPDVVHT----HNLSG---------------LGASLLDAARDLGIPVV--HTLHDYWLLCPRQ---FLFKKGG 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 161 DR-----AKLADLV---GIDYKQTIVIDGaGINPEIYKysLEQQRDVP---VVLFASRMLWSKGLGDLIEAKKILSNKNI 229
Cdd:cd03823   145 DAvlapsRFTANLHeanGLFSARISVIPN-AVEPDLAP--PPRRRPGTerlRFGYIGRLTEEKGIDLLVEAFKRLPREDI 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 230 HFTlnVAGILVENDkdaiplatIQKWQSEGVINWLG--HCSNVFDLIEESNIVALPSVYAEGVPRILLEASSVGRACIAY 307
Cdd:cd03823   222 ELV--IAGHGPLSD--------ERQIEGGRRIAFLGrvPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIAS 291
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1819699085 308 DVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRI 358
Cdd:cd03823   292 DLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPR 342
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
188-376 3.17e-08

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 55.02  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 188 IYKYSLEQQRDVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGILVENDKDA--IPLATIQKWQSEGVINWLG 265
Cdd:cd03792   186 YLEKPFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGsvVYEEVMEYAGDDHDIHVLR 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 266 HCSN--VFDLIEESNIVALPSVYAEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSksVEELAEKLGFLLDN 343
Cdd:cd03792   266 LPPSdqEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAVRILRLLTD 343
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1819699085 344 PETRVAMGINGRKRIQDKFssvmIINKTLKTYL 376
Cdd:cd03792   344 PELRRKMGLAAREHVRDNF----LITGNLRAWL 372
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
279-363 9.52e-08

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 49.52  E-value: 9.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 279 IVALPSVYAEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSksVEELAEKLGFLLDNPETRVAMGINGRKRI 358
Cdd:pfam13524   1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRD--PEELAEKIRYLLEHPEERRAIAAAGRERV 78

                  ....*
gi 1819699085 359 QDKFS 363
Cdd:pfam13524  79 LAEHT 83
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
220-364 1.05e-07

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 53.23  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 220 AKKILSNKNIHFTLNVagilvendkdaiplatiqkwQSEGVINW-LGHCSNVFDLIEESnivalpsvyaEGVPRILLEAS 298
Cdd:cd04946   276 AENKLENVKVNFTGEV--------------------SNKEVKQLyKENDVDVFVNVSES----------EGIPVSIMEAI 325
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819699085 299 SVGRACIAYDVGGCDSLIINNYNGLI-VKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSS 364
Cdd:cd04946   326 SFGIPVIATNVGGTREIVENETNGLLlDKDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNA 392
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
26-179 7.29e-07

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 48.68  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085  26 AIAARDAGYEIHIISHFVDDKIAEKFRTLGFVCHNIPLVAQSFnvLIFFRAFSKARKIIQNINPDLLHCITIKPCLIGGF 105
Cdd:pfam13439  11 ARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRL--LRSLAFLRRLRRLLRRERPDVVHAHSPFPLGLAAL 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819699085 106 -LAKSTHRPVILSFVGLGRVFSAESACLKLLRSFTVMAYKYIAsNKCSLFMFEHDKDRAKLADLVGIDYKQTIVI 179
Cdd:pfam13439  89 aARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRLL-RRADRVIAVSEAVADELRRLYGVPPEKIRVI 162
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
183-376 1.30e-06

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 49.75  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 183 GINPEIYKYSLEQQR----------DVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAGilvENDKDAIPLATI 252
Cdd:cd04951   162 GIDLNKFKKDINVRLkirnklnlknDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAG---DGPLRNELERLI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 253 QKWQSEGVINWLGHCSNVFDLIEESNIVALPSVYaEGVPRILLEASSVGRACIAYDVGGCDSlIINNYNGLIVKSKSvEE 332
Cdd:cd04951   239 CNLNLVDRVILLGQISNISEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAE-VVGDHNYVVPVSDP-QL 315
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1819699085 333 LAEKLG-FLLDNPETRVAMGiNGRKRIQDKFSSVMIINKTLKTYL 376
Cdd:cd04951   316 LAEKIKeIFDMSDEERDILG-NKNEYIAKNFSINTIVNEWERLYS 359
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
249-378 7.29e-06

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 47.35  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 249 LATIQKWQSE-GVIN---WLGHCSNVFDLIEESNIVALPSvYAEGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLI 324
Cdd:cd04962   238 RVPAEELARElGVEDrvlFLGKQDDVEELLSIADLFLLPS-EKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFL 316
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1819699085 325 VKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSVMIINKTLKTYLDV 378
Cdd:cd04962   317 SDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
293-361 2.97e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 45.75  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819699085 293 ILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDK 361
Cdd:cd03814   283 VVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERY 351
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
290-363 3.42e-05

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 45.66  E-value: 3.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819699085 290 VPrilLEASSVGRACIAYDVGG-CDSlIINNYNGLIVkSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFS 363
Cdd:cd03805   315 VP---LEAMYAGKPVIACNSGGpLET-VVEGVTGFLC-EPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFS 384
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
203-337 8.91e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 43.93  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 203 LFASRMLW--SKGLGDLIEAkkiLSNKNIHFTLNVAGilvENDKDAIPLATIQKWQSEGVINWLGHCSN----VFDLIEE 276
Cdd:PRK09922  184 LYVGRLKFegQKNVKELFDG---LSQTTGEWQLHIIG---DGSDFEKCKAYSRELGIEQRIIWHGWQSQpwevVQQKIKN 257
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819699085 277 SNIVALPSVYaEGVPRILLEASSVGRACIAYD-VGGCDSLIINNYNGLIVKSKSVEELAEKL 337
Cdd:PRK09922  258 VSALLLTSKF-EGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKL 318
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
288-375 3.04e-04

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 42.71  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 288 EGVPRILLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVE--ELAEKLGFLLDNPETRVAMGINGRKRIQDKFSSV 365
Cdd:PRK15179  602 EGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTapDVAEALARIHDMCAADPGIARKAADWASARFSLN 681
                          90
                  ....*....|
gi 1819699085 366 MIINKTLKTY 375
Cdd:PRK15179  682 QMIASTVRCY 691
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
294-364 3.33e-03

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 39.27  E-value: 3.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819699085 294 LLEASSVGRACIAYDVGGCDSLIINNYNGLIVKSKSVEELAEKLGFLLDNPETRVAMGINGRKRIQDKFSS 364
Cdd:cd03818   317 LLEAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSL 387
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
162-350 6.44e-03

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 38.13  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 162 RAKLADLVGIDYKQTIVID-GAGINPEIYKYSLE---QQRDVPVVLFASRMLWSKGLGDLIEAKKILSNKNIHFTLNVAG 237
Cdd:cd03822   146 RFLLVRIKLIPAVNIEVIPhGVPEVPQDPTTALKrllLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAG 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819699085 238 ILVEN---------DKDAIPLATIQK---WQSEGVINwlghcSNVFDLIEESNIVALPsvY---AEGVPRILLEASSVGR 302
Cdd:cd03822   226 ELHPSlaryegeryRKAAIEELGLQDhvdFHNNFLPE-----EEVPRYISAADVVVLP--YlntEQSSSGTLSYAIACGK 298
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1819699085 303 ACIAYDVGGCDSLIINNyNGLIVKSKSVEELAEKLGFLLDNPETRVAM 350
Cdd:cd03822   299 PVISTPLRHAEELLADG-RGVLVPFDDPSAIAEAILRLLEDDERRQAI 345
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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